Proteolytic processing of the p2/nucleocapsid cleavage site is critical for human immunodeficiency virus type 1 RNA dimer maturation.
about
Nucleic acid binding and chaperone properties of HIV-1 Gag and nucleocapsid proteinsDeterminants of Genomic RNA Encapsidation in the Saccharomyces cerevisiae Long Terminal Repeat Retrotransposons Ty1 and Ty3HIV Genome-Wide Protein Associations: a Review of 30 Years of ResearchWrapping up the bad news: HIV assembly and releaseThe choreography of HIV-1 proteolytic processing and virion assemblyHIV-1 protease and reverse transcriptase control the architecture of their nucleocapsid partnerImperfect DNA mirror repeats in the gag gene of HIV-1 (HXB2) identify key functional domains and coincide with protein structural elements in each of the mature proteins.The inhibition of assembly of HIV-1 virus-like particles by 3-O-(3',3'-dimethylsuccinyl) betulinic acid (DSB) is counteracted by Vif and requires its Zinc-binding domain.Understanding HIV-1 protease autoprocessing for novel therapeutic development.Analysis of the contribution of reverse transcriptase and integrase proteins to retroviral RNA dimer conformation.Effects of Gag mutation and processing on retroviral dimeric RNA maturation.Proline residues within spacer peptide p1 are important for human immunodeficiency virus type 1 infectivity, protein processing, and genomic RNA dimer stability.Cofactors for human immunodeficiency virus type 1 cDNA integration in vitroHIV-1 RNA dimerization: It takes two to tangoThe conformation of the mature dimeric human immunodeficiency virus type 1 RNA genome requires packaging of pol protein.New findings in cleavage sites variability across groups, subtypes and recombinants of human immunodeficiency virus type 1The dimer initiation sequence stem-loop of human immunodeficiency virus type 1 is dispensable for viral replication in peripheral blood mononuclear cells.The allosteric HIV-1 integrase inhibitor BI-D affects virion maturation but does not influence packaging of a functional RNA genomeEffects of blocking individual maturation cleavages in murine leukemia virus gag.Gag non-cleavage site mutations contribute to full recovery of viral fitness in protease inhibitor-resistant human immunodeficiency virus type 1.Dimerization of retroviral RNA genomes: an inseparable pair.HIV-2 genome dimerization is required for the correct processing of Gag: a second-site reversion in matrix can restore both processes in dimerization-impaired mutant virusesVif is a RNA chaperone that could temporally regulate RNA dimerization and the early steps of HIV-1 reverse transcription.Structure/function mapping of amino acids in the N-terminal zinc finger of the human immunodeficiency virus type 1 nucleocapsid protein: residues responsible for nucleic acid helix destabilizing activityIn vitro synthesis of long DNA products in reactions with HIV-RT and nucleocapsid protein.Suboptimal inhibition of protease activity in human immunodeficiency virus type 1: effects on virion morphogenesis and RNA maturationA new role for HIV nucleocapsid protein in modulating the specificity of plus strand priming.Nucleocapsid protein function in early infection processes.The A-rich RNA sequences of HIV-1 pol are important for the synthesis of viral cDNA.The conserved carboxy terminus of the capsid domain of human immunodeficiency virus type 1 gag protein is important for virion assembly and release.Tumultuous relationship between the human immunodeficiency virus type 1 viral infectivity factor (Vif) and the human APOBEC-3G and APOBEC-3F restriction factors.Targeting human immunodeficiency virus type 1 assembly, maturation and budding.Visualization of human immunodeficiency virus protease inhibition using a novel Förster resonance energy transfer molecular probe.Role of Gag in HIV Resistance to Protease InhibitorsThe relationship between HIV-1 genome RNA dimerization, virion maturation and infectivity.The dimer interfaces of protease and extra-protease domains influence the activation of protease and the specificity of GagPol cleavage.Variability at human immunodeficiency virus type 1 subtype C protease cleavage sites: an indication of viral fitness?Design of a trans protease lentiviral packaging system that produces high titer virus.Dimerisation of HIV-2 genomic RNA is linked to efficient RNA packaging, normal particle maturation and viral infectivity.Recovery of fitness of a live attenuated simian immunodeficiency virus through compensation in both the coding and non-coding regions of the viral genome.
P2860
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P2860
Proteolytic processing of the p2/nucleocapsid cleavage site is critical for human immunodeficiency virus type 1 RNA dimer maturation.
description
2001 nî lūn-bûn
@nan
2001 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Proteolytic processing of the ...... s type 1 RNA dimer maturation.
@ast
Proteolytic processing of the ...... s type 1 RNA dimer maturation.
@en
type
label
Proteolytic processing of the ...... s type 1 RNA dimer maturation.
@ast
Proteolytic processing of the ...... s type 1 RNA dimer maturation.
@en
prefLabel
Proteolytic processing of the ...... s type 1 RNA dimer maturation.
@ast
Proteolytic processing of the ...... s type 1 RNA dimer maturation.
@en
P2093
P2860
P1433
P1476
Proteolytic processing of the ...... us type 1 RNA dimer maturation
@en
P2093
H G Kraeusslich
J A Marshall
M Shehu-Xhilaga
R Swanstrom
P2860
P304
P356
10.1128/JVI.75.19.9156-9164.2001
P50
P577
2001-10-01T00:00:00Z